Nε-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity

Sandy Thao, Chien Sheng Chen, Heng Zhu, Jorge C. Escalante-Semerena

Research output: Contribution to journalArticle

Abstract

Evidence suggesting that eukaryotes and archaea use reversible Nε-lysine (Nε-Lys) acetylation to modulate gene expression has been reported, but evidence for bacterial use of Nε-Lys acetylation for this purpose is lacking. Here, we report data in support of the notion that bacteria can control gene expression by modulating the acetylation state of transcription factors (TFs). We screened the E. coli proteome for substrates of the bacterial Gcn5-like protein acetyltransferase (Pat). Pat acetylated four TFs, including the RcsB global regulatory protein, which controls cell division, and capsule and flagellum biosynthesis in many bacteria. Pat acetylated residue Lys180 of RcsB, and the NAD+-dependent Sir2 (sirtuin)-like protein deacetylase (CobB) deacetylated acetylated RcsB (RcsBAc), demonstrating that Nε-Lys acetylation of RcsB is reversible. Analysis of RcsBAc and variant RcsB proteins carrying substitutions at Lys180 provided biochemical and physiological evidence implicating Lys180 as a critical residue for RcsB DNA-binding activity. These findings further the likelihood that reversible Ne-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells.

Original languageEnglish (US)
Article numbere15123
JournalPLoS One
Volume5
Issue number12
DOIs
StatePublished - 2010

Fingerprint

Acetylation
acetylation
Lysine
lysine
Transcription Factors
transcription factors
acetyltransferases
Acetyltransferases
DNA
Gene expression
Proteins
proteins
Sirtuins
Bacteria
Gene Expression
gene expression
Flagella
Archaea
bacteria
regulatory proteins

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Nε-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity. / Thao, Sandy; Chen, Chien Sheng; Zhu, Heng; Escalante-Semerena, Jorge C.

In: PLoS One, Vol. 5, No. 12, e15123, 2010.

Research output: Contribution to journalArticle

Thao, Sandy ; Chen, Chien Sheng ; Zhu, Heng ; Escalante-Semerena, Jorge C. / Nε-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity. In: PLoS One. 2010 ; Vol. 5, No. 12.
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